1IOS

STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION

Summary for 1IOS

Entry DOI	10.2210/pdb1ios/pdb
Related	1IOQ 1IOR 1IOT
Descriptor	LYSOZYME C (2 entities in total)
Functional Keywords	hydrolase, glycosidase, bacteriolytic enzyme
Biological source	Gallus gallus (chicken)
Cellular location	Secreted: P00698
Total number of polymer chains	1
Total formula weight	14347.14
Authors	Ohmura, T.,Ueda, T.,Ootsuka, K.,Saito, M.,Imoto, T. (deposition date: 2001-03-28, release date: 2001-04-11, Last modification date: 2024-10-23)
Primary citation	Ohmura, T.,Ueda, T.,Ootsuka, K.,Saito, M.,Imoto, T. Stabilization of hen egg white lysozyme by a cavity-filling mutation. Protein Sci., 10:313-320, 2001 Cited by PubMed Abstract: Stabilization of a protein using cavity-filling strategy has hardly been successful because of unfavorable van der Waals contacts. We succeeded in stabilizing lysozymes by cavity-filling mutations. The mutations were checked by a simple energy minimization in advance. It was shown clearly that the sum of free energy change caused by the hydrophobicity and the cavity size was correlated very well with protein stability. We also considered the aromatic-aromatic interaction. It is reconfirmed that the cavity-filling mutation in a hydrophobic core is a very useful method to stabilize a protein when the mutation candidate is selected carefully. PubMed: 11266617 DOI: 10.1110/ps.37401 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.76 Å)

Structure validation